Beta-crystallin B2 is a protein that in humans is encoded by the CRYBB2 gene.[5][6][7]

CRYBB2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCRYBB2, CCA2, CRYB2, CRYB2A, CTRCT3, D22S665, crystallin beta B2
External IDsOMIM: 123620; MGI: 88519; HomoloGene: 420; GeneCards: CRYBB2; OMA:CRYBB2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000496

NM_007773

RefSeq (protein)

NP_000487

NP_031799

Location (UCSC)Chr 22: 25.21 – 25.23 MbChr 5: 113.21 – 113.22 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N-terminal and C-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta basic group member, is part of a gene cluster with beta-A4, beta-B1, and beta-B3. A chain-terminating mutation was found to cause type 2 cerulean cataracts.[7]

Interactions

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CRYBB2 has been shown to interact with Hsp27,[8] CRYGC,[8] CRYAA[8] and CRYAB.[8]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000244752Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000042240Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Litt M, Carrero-Valenzuela R, LaMorticella DM, Schultz DW, Mitchell TN, Kramer P, Maumenee IH (Jul 1997). "Autosomal dominant cerulean cataract is associated with a chain termination mutation in the human beta-crystallin gene CRYBB2". Hum Mol Genet. 6 (5): 665–8. doi:10.1093/hmg/6.5.665. PMID 9158139.
  6. ^ Chambers C, Russell P (Dec 1993). "Sequence of the human lens beta B2-crystallin-encoding cDNA". Gene. 133 (2): 295–9. doi:10.1016/0378-1119(93)90655-M. PMID 8224918.
  7. ^ a b "Entrez Gene: CRYBB2 crystallin, beta B2".
  8. ^ a b c d Fu L, Liang JJ (February 2002). "Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay". J. Biol. Chem. 277 (6): 4255–60. doi:10.1074/jbc.M110027200. PMID 11700327.
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Further reading

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